ID A0A2T7FY89_9RHOB Unreviewed; 755 AA.
AC A0A2T7FY89;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=DC363_04560 {ECO:0000313|EMBL:PVA07133.1};
OS Thalassorhabdomicrobium marinisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thalassorhabdomicrobium.
OX NCBI_TaxID=2170577 {ECO:0000313|EMBL:PVA07133.1, ECO:0000313|Proteomes:UP000244817};
RN [1] {ECO:0000313|EMBL:PVA07133.1, ECO:0000313|Proteomes:UP000244817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH-SD16 {ECO:0000313|EMBL:PVA07133.1,
RC ECO:0000313|Proteomes:UP000244817};
RA Ji X.;
RT "Pelagivirga bohaiensis gen. nov., sp. nov., a bacterium isolated from the
RT Bohai Sea.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of ribonucleotides to
CC deoxyribonucleotides. May function to provide a pool of
CC deoxyribonucleotide precursors for DNA repair during oxygen limitation
CC and/or for immediate growth after restoration of oxygen.
CC {ECO:0000256|RuleBase:RU364064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU364064};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922,
CC ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVA07133.1}.
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DR EMBL; QCYG01000003; PVA07133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7FY89; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000244817; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR NCBIfam; TIGR02504; NrdJ_Z; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064};
KW Reference proteome {ECO:0000313|Proteomes:UP000244817}.
FT DOMAIN 8..79
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 85..551
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 755 AA; 82559 MW; CE80B5AEAF65C3BE CRC64;
MTRFAAPIAE QIWDMKYRLK DAEGAPIDAT VEDTWSRVAK SLASVEKDPA AWEPKFYAAL
EDFKYLPAGR ITAGAGTDRS VTLFNCFVMG TIPDTMSGIF ENLREAALTM QQGGGIGYDF
STIRPRGALV KGVAADASGP LSFMDVWDAM CRTIMSAGSR RGAMMATMRC DHPDVEDFIT
AKSDPARLRM FNMSVLVTDP FMEAVKADKA WDLVWEGATI KTVKARDLWN SIMQSTYDQA
EPGVIFIDRI NEMNNLNYVE TIAATNPCGE QPLPPYGACL LGSVNLARLV STPFEDGAGI
DDAELSDLVA TAVRMMDNVV DASNFPLEAQ AQEAAAKRRI GLGVTGLADA LLMVGLRYGS
EEAARQTEHW MKQVARAAYL ASVELAKEKG AFPLFDAEKY LASGTMMQMD DDVRDAIREH
GIRNALLTSV APTGTISLYA GNVSSGIEPV FAYAYTRKVL QKDGTRTEEE VVDYAVKLWR
DLKGDAELPD YFVNAQTLPA LDHVRMQAAA QKWVDSSISK TINVPEDISF DDFKEVYMEA
WDSGCKGCTT YRPNDVTGSV LSVESEKEAA PEVVADENAG DVIYMTEPLD RPGELTGQTY
KLKWPDSEHA IYITVNDIQH QGQQRPFEVF INSKNMEHFA WTVALTRMIS AVFRRGGDVS
FVVEELKAVF DPRGGAWMNG KYVPSILAAI GSVIEKHMIS TGFLAGEGLG LKSDPQADVV
SMKPKGKACS SCGSYELRMI EGCMTCGSCG HSKCG
//
